EC Number   |
General Information |
Reference |
|---|
   3.6.1.56 | malfunction |
MTH1-null mouse embryo fibroblasts are highly susceptible to cell dysfunction and death caused by exposure to H2O2, with condensed nuclei and degenerated mitochondria in which electron dense deposits are seen in place of intact cristae. The cell death observed is not dependent on either poly(ADP-ribose) polymerase or caspases. A continuous accumulation of 8-oxoG, both in the nuclear and mitochondrial DNA, is observed after exposure to H2O2. All of the H2O2-induced alterations observed in MTH1-null MEFs are effectively suppressed by the expression of wild-type human MTH1 |
716299 |
| 3.6.1.56 | malfunction |
the knockdown of the MTH1, MTH2, and NUDT5 proteins increases the A:T to C:G substitution mutations induced by 8-hydroxy-dGTP. In addition, the increase in the induced mutation frequency is more evident in the triple-knockdown cells |
715083 |
| 3.6.1.56 | physiological function |
all three of the human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP |
715083 |
| 3.6.1.56 | physiological function |
is produced in cells by reactive oxygen species normally formed during cellular metabolic processes. This oxidized base can pair with both adenine and cytosine, and thus the existence of this base in messenger RNA would cause translational errors. The elimination of 8-oxoguanine-containing ribonucleotides from the precursor pool is important to ensure accurate protein synthesis. Both NUDT5 and MTH1 are involved in this process in human cells |
716365 |
| 3.6.1.56 | physiological function |
MTH1 efficiently suppresses the accumulation of 8-oxoguanine in both cellular DNA and RNA in the hippocampus, especially in microglia, caused by excitotoxicity (caused by the systemic administration of kainate) |
669948 |
| 3.6.1.56 | physiological function |
MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxydATP, and 2-hydroxy-rATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration |
715460 |
| 3.6.1.56 | physiological function |
MTH1 protects the dopamine neurons from oxidative damage in the nucleic acids, especially in the mitochondrial DNA of striatal nerve terminals of dopamine neurons |
668195 |
| 3.6.1.56 | physiological function |
MTH1, a major sanitizing enzyme for oxidized nucleotide pools plays a crucial role by suppressing their accumulation in cellular DNA. In addition to oxidized purine deoxyribonucleoside triphosphates, MTH1 efficiently hydrolyzes oxidized purine ribonucleoside triphosphates such as 2-hydroxy-ATP, 8-oxo-ATP and, to a lesser extent, 8-oxo-GTP |
716299 |
| 3.6.1.56 | physiological function |
the enzyme prevents the incorporation of oxidized nucleotides such as 2-hydroxy-ATP and 8-oxo-dGTP during DNA replication by hydrolysing them into their corresponding monophosphates |
756426 |
